TY - JOUR
TI - A Pan Photoaffinity Probe for Detecting Active Forms of Matrix Metalloproteinases
AU - Nury, C.
AU - Czarny, B.
AU - Cassar-Lajeunesse, E.
AU - Georgiadis, D.
AU - Bregant, S.
AU - Dive, V.
JO - ChemBioChem
PY - 2013
VL - 14
TODO - 1
SP - 107-114
PB - 
SN - 1439-4227, 1439-7633
TODO - 10.1002/cbic.201200583
TODO - collagenase 3;  gelatinase A;  gelatinase B;  macrophage elastase;  matrix metalloproteinase;  matrix metalloproteinase 14;  neutrophil collagenase;  stromelysin;  tritium, article;  chemical modification;  controlled study;  cross linking;  enzyme mechanism;  photoaffinity labeling;  priority journal;  radioactivity;  radiography, Azides;  Azirines;  Catalytic Domain;  Cross-Linking Reagents;  Humans;  Light;  Matrix Metalloproteinases;  Molecular Probe Techniques;  Photoaffinity Labels
TODO - A photoaffinity probe based on the scaffold of a potent broad-spectrum phosphinic peptide inhibitor of matrix metalloproteinases (MMPs) has been developed. A photolabile diazirine group for covalent modification of MMP active forms was incorporated at the P1′ position, and a tritium radioactive label for the sensitive detection of MMP covalent adducts by radioimaging was attached. The probe was characterized on seven catalytic domains of human MMPs (MMP-2, -3, -8, -9, -12, -13 and -14) and was found to display nanomolar affinities towards this set of MMPs, covalently modifying them with crosslinking yields varying from 12 to 58%, thus leading to highly sensitive detection of these MMPs. In a complex proteome complemented with four recombinant MMPs (MMP-2, -9, -12 and -13), this probe enabled their simultaneous detection with a threshold of few femtomoles and low background labelling. Those properties should make this new pan-activity-based MMP probe a valuable tool for the detection of MMP active forms from biological fluids or tissue extracts. © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
ER -